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Description
The superoxide dismutase family is composed of three metalloenzymes (SOD-1, SOD-2 and SOD-3) that catalyze the oxido-reduction of reactive oxygen species (ROS) such as superoxide anion. The SOD-2 precursor is a 222 AA protein that is encoded by nuclear chromatin, synthesized in the cytosol and imported posttranslationally into the mitochondrial matrix. Unlike SOD-1, which is a homodimeric cytosolic Cu-Zn enzyme, SOD-2 is a homotetrameric manganese enzyme (also known as MnSOD) that functions in the mitochondrion. ROS are implicated in a wide range of degenerative processes, including Alzheimer's disease, Parkinson's disease and ischemic heart disease. Homozygous mutant mice, which lack SOD-2, exhibit dilated cardiomyopathy, accumulation of lipid in liver and skeletal muscle, metabolic acidosis, oxidative DNA damage and respiratory chain deficiencies in heart and skeletal muscle. Polymorphisms in the SOD-2 gene have also been implicated in nonfamilial, idiopathic, dilated cardiomyopathy in humans.